Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.9.3.1 (cytochrome oxidase)
8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Brain mitochondrial enzyme activities were examined in 15-day-old suckling mice which were daily injected with D-penicillamine (DP), a chelating agent of copper. Newborn mice treated with DP (1 g/kg/day) showed retarded weight gain, hyperelasticity of skin, and a bizarre forelimb posture with subcutaneous edema on experimental day (ED) 7. Paraparesis or dragging of the hindlimbs was observed by ED 15. Brain copper contents of DP-treated mice decreased to 34% of the controls of ED 15. Cytochrome c oxidase activity (complex IV) in the brain showed 51% decrease of the controls, on the contrary, rotenone-sensitive NADH cytochrome c reductase (complex I + III) and succinate cytochrome c reductase (complex II + III) were normal. Histochemistry of cytochrome c oxidase in the cerebellum of DP-treated mice disclosed diffuse reduction of staining, especially in Purkinje cells. These data show that DP-induced copper deficiency in the brain subsequently disturbs mitochondrial electron transport system, selectively cytochrome c oxidase activity. This seems to be a useful animal model not only for Menkes' kinky hair disease but also for mitochondrial encephalomyopathy.
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PMID:D-penicillamine-induced copper deficiency in suckling mice: neurological abnormalities and brain mitochondrial enzyme activities. 217 57

The gene organization of the Peking duck mitochondrial (mt)DNA has been deduced through heterologous hybridization using different cloned fragments of the chicken or Japanese quail mitochondrial genome as probes. As in the chicken, and other gallinaceous birds, the Peking duck mtDNA displays a novel gene order which differs from that of other vertebrates by the unusual localization of the tRNA(Glu) and ND6 genes next to the displacement (D) loop region of the molecule. The position of these genes with respect to the mitochondrial D-loop region, the cytochrome oxidase subunits I, II and III, the NADH dehydrogenase subunit I and the ribosomal (r) RNAs, was confirmed by the partial nucleotide sequence of cloned mtDNA fragments.
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PMID:Gene organization of the Peking duck mitochondrial genome. 239 Jul 86

The assembly of mitochondrially and cytoplasmically translated subunits of NADH dehydrogenase in the inner mitochondrial membrane was studied in rat hepatoma cultures. A polyclonal antibody to the purified bovine heart holoenzyme, which reacted with comigrating proteins of both rat liver and hepatoma mitochondria on immunoblots, precipitated 25-30 [35S]methionine-labeled proteins from hepatoma cell lysates. Six of these were sensitive to an inhibitor of mitochondrial translation (chloramphenicol), resistant to an inhibitor of cytosolic translation (cycloheximide), and were not present in cytochrome oxidase. By these criteria, six NADH dehydrogenase subunits are identified as being translated on mitochondrial ribosomes. The metabolic properties of the three most prominent of these at 51, 43, and 11 kDa were studied in more detail. Mitochondrial and nuclear-coded polypeptides assemble into NADH dehydrogenase at different rates as measured by incorporation of pulse-labeled proteins into immunoprecipitable enzyme. Nuclear-coded, imported polypeptides appear immediately after a pulse with [35S]methionine and retain constant stoichiometry. Mitochondrially coded proteins, although rapidly translated, appear at peak levels at different times between 0 and 12 h of chase in the immunoprecipitated enzyme. Ongoing synthesis and import of nuclear-coded proteins is necessary for mitochondrially coded proteins to be assembled. Excess, unassembled mitochondrially translated subunits are degraded in an oligomycin-sensitive manner. These data are consistent with a model in which a scaffold of imported proteins forms the inner core of the enzyme, and later arriving mitochondrially translated proteins attach to the scaffold in a time-dependent manner.
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PMID:Respiratory chain-linked NADH dehydrogenase. Mechanisms of assembly. 239 60

Previous studies have shown that behavioral and neurophysiological responses to tastes develop during rat's postnatal life. The present experiments evaluated morphological and metabolic development of neurons in the gustatory zone of the caudal parabrachial nucleus (PBNc) of rat. Histological reconstruction studies were conducted to establish coordinate systems for PBNc gustatory zones in developing rats. Reliability of coordinate systems were evaluated in separate experiments following infusions of horseradish peroxidase in the thalamic taste area. Morphological and Golgi impregnation studies were performed to characterize neuronal and dendritic architecture in PBNc gustatory zones defined by coordinates. Conventional histochemical studies were performed for the mitochondrial respiratory enzymes cytochrome C oxidase (CO; EC 1.9.3.1) succinate dehydrogenase (SDH; EC 1.3.99.1), and NADH-dehydrogenase (NADH-DH; EC 1.6.99.3). Results show that two somatic morphologies can be statistically characterized in PBNc gustatory zones: Multipolar somatic types and fusiform somatic types. Multipolar and fusiform neurons of neonatal and adult rats project axons to the thalamic taste area, and dendrites of these neurons grow extensively between approximately 16 days after birth to approximately 35 days after birth. Activity of CO, SDH, and NADH-DH increases in the PBNc gustatory zones during the period of dendritic growth, and continues to increase slightly to approximately 45 days. These results provide the first demonstration of postnatal morphological and metabolic developmental in a central gustatory relay. Postnatal development of gustatory system therefore appears similar to that reported for other sensory systems, to the extent that morphological and metabolic development accompanies the ontogeny of taste responses.
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PMID:Postnatal development of the parabrachial gustatory zone in rat: dendritic morphology and mitochondrial enzyme activity. 246 23

Morphological and metabolic development of the gustatory zone of the rostral nucleus of the solitary tract (NST) was examined in rat. Transganglionic transport of horseradish peroxidase (HRP) was used to visualize the organization of gustatory projections to the rostral gustatory NST in rats aged postnatal day 1 (P1) to P34. Golgi impregnation studies were performed to analyze morphological development of dendrites in regions of the rostral NST that were identified as anterior tongue terminal fields. Results demonstrate that afferent fibers of the anterior tongue project to the rostral NST in rats as young as P1. The volume of NST terminal fields increased from P1 to approximately P16-P20, and was adult-like after approximately P20. Developmental increases in terminal field volume resulted from a preferential expansion in the rostrocaudal plane. Planar length of first-order dendrites associated with fusiform, multipolar, and ovoid neurons, and second-order dendrites of fusiform and ovoid neurons, increased approximately three-fold between P4 and P16-20. First-order dendritic length for all morphological types was adult-like after approximately 20-25 days of age, whereas second-order dendritic length of multipolar neurons increased significantly between P30 and P60-70. Histochemical studies confirmed that activity of the mitochondrial respiratory enzymes cytochrome c oxidase (EC 1.9.3.1), succinate dehydrogenase (EC 1.3.99.1), and NADH-dehydrogenase (EC 1.6.99.3) increased monotonically during the developmental period in which planar growth of first-order dendrites was observed. The present results, in combination with results from previous studies, indicate that morphological and metabolic development fo the NST occurs concomitantly with morphological development of taste receptors and peripheral gustatory nerves.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Postnatal development of the rostral solitary nucleus in rat: dendritic morphology and mitochondrial enzyme activity. 246 1

The effect of Ca2+-homopantothenate (HOPA) treatment (250 mg/kg for 5 d) has been studied by evaluating the specific activity of enzymes related to: glycolytic pathway (hexokinase, phosphofructokinase, pyruvate kinase, lactate dehydrogenase), tricarboxylic acid cycle (citrate synthase, malate dehydrogenase), mitochondrial electron transfer chain (succinate dehydrogenase, cytochrome oxidase), NADH redox state (NADH cytochrome c reductase), acetylcholine metabolism (acetylcholinesterase), and glutamate metabolism (glutamate dehydrogenase). The enzymatic activity assays were performed on homogenate in toto, nonsynaptic mitochondria and synaptosomes isolated from: cerebral cortex, hippocampus, striatum, hypothalamus, medulla oblongata, and cerebellum of normoxic rats and rats submitted to intermittent normobaric hypoxia (90:10, N2:O2). In normoxic rats, HOPA was unable to induce any modification. Hypoxia per se induced a decrease in the activity of synaptosomal cytochrome oxidase in cerebral cortex, hippocampus, and cerebellum.
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PMID:Effect of Ca2+-homopantothenate and mild hypoxia on some enzyme activities evaluated in subcellular fractions from different rat brain regions. 254 16

When pharmacological or basic neurochemical systematic characterization of mitochondrial enzymatic systems correlated to energy transduction processes is attempted, studies must be based on subcellular fractions with a high degree of purity from specific brain areas and from individual animals. Distinct populations of mitochondria heterogenous with respect to biochemical enzyme characteristics from rat brain hippocampus are described. Two mitochondrial populations were derived from synaptosomes by lysis and a third consists of free non-synaptic mitochondria. The maximum rate of some cerebral enzyme activities which are part of energy transduction (citrate synthase, malate dehydrogenase; total NADH-cytochrome c reductase, cytochrome oxidase) and amino acid metabolism (glutamate dehydrogenase) were tested on these mitochondrial populations of 8- and 16-week-old rats. A comprehensive analysis of the data suggests that extensive but highly diversified catalytic expressions of the enzymes studied occur in the hippocampus. This is true even when a short period of the rat life span is studied. Hence the varying pattern of evolution of the differing cerebral mitochondria, probably a consequence of different metabolic functions, should be taken into account in any pharmacological study on these systems.
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PMID:Enzyme activities in perikaryal and synaptic mitochondrial fractions from rat hippocampus during development. 255 73

Rotenone-sensitive NADH dehydrogenase activity and Lubrol stimulation of cytochrome oxidase activity were measured to assess the opposite membrane polarity of beef heart mitoplast and inside-out particle preparations. The ATP-Pi exchange activity of mitoplasts was not affected by their incubation at pH 8.9 in the presence of 5 mM EDTA (a treatment known to extract coupling factor B (F beta) from submitochondrial particles), nor was it stimulated by the addition of F beta to intact and alkaline treated mitoplast preparations. In contrast, the exchange activity of inside-out particles was decreased 18 fold by the alkaline/EDTA treatment and was almost completely restored by the addition of F beta to F beta-depleted particles. From these results it is concluded that in beef heart mitochondria, the coupling factor F beta is bound to the matrix-side of the inner mitochondrial membrane.
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PMID:Evidence that coupling factor B is bound to the matrix side of the inner mitochondrial membrane. 256 42

We isolated from a HeLa genomic library 38 plaques that hybridized to total mitochondrial (mt) DNA isolated from human placenta. One clone (HLmt-17.8) hybridized to a 740 base-pair (12 S ribosomal RNA gene and displacement loop) mtDNA probe and was characterized in more detail. Within its 17.8 x 10(3) base-pair insert a 1.6 x 10(3) base-pair mtDNA fragment was similar to three non-sequential coding genes of human mtDNA, including a part of the 12 S ribosomal RNA (684-971), the cytochrome oxidase I (6553-7302), and two NADH dehydrogenase [ND4L/ND4] (10,606-11,159). The similarity to human mtDNA sequences was 92.0%, 92.3% and 92.4%, respectively, the highest degree of similarity to human mtDNA so far reported. This is also the first report of several adjacent mtDNA-like sequences in cellular chromosomes. The mtDNA-like sequences in HLmt-17.8 was found in the DNAs of human placenta, freshly isolated human leukocytes, foreskin and several human cell lines; but it was not present in other primates or lower organisms. The HLmt-17.8 mtDNA-like region appears to be a pseudogene that transferred into the nucleus in humans more recently than nine million years ago.
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PMID:Three separate mitochondrial DNA sequences are contiguous in human genomic DNA. 261 44

We report two brothers with a previously undescribed type of mitochondrial encephalomyopathy and associated aminoacidopathy. Both have growth failure, progressive intellectual decline, deafness, neurologic dysfunction, exercise intolerance, lactic acidosis, and abnormal plasma and cerebrospinal fluid amino acid levels (elevated levels of alanine and low levels of threonine, methionine, citrulline, tryptophan, ornithine, arginine, and lysine). A muscle biopsy specimen taken from the younger, more severely affected brother showed abnormal mitochondrial morphology. Activities of the following enzymes in cultured fibroblasts from both boys were normal: pyruvate dehydrogenase, pyruvate carboxylase, phosphoenolpyruvate carboxykinase, cytochrome oxidase, reduced nicotinamide-adenine dinucleotide-cytochrome c reductase, and succinate cytochrome c reductase. Fibroblast mitochondria from the younger boy showed undetectable (less than 1% of control values) adenosine triphosphate synthesis with pyruvate and malate, whereas adenosine triphosphate synthesis with succinate was 70% of control values. These data indicate probably deficient activity of complex I of the electron transport chain. The boys' mother has progressive neurosensory hearing loss; their sister is clinically normal. Both mother and sister have many of the biochemical abnormalities found in the boys. It is possible, but not proved, that this disorder is inherited through maternal mitochondria.
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PMID:Mitochondrial encephalomyopathy with associated aminoacidopathy in a male sibship. 273 99


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